AKAP3_HUMAN
ID AKAP3_HUMAN Reviewed; 853 AA.
AC O75969; O75945; Q86X01; Q9UM61;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=A-kinase anchor protein 3;
DE Short=AKAP-3;
DE AltName: Full=A-kinase anchor protein 110 kDa;
DE Short=AKAP 110;
DE AltName: Full=Cancer/testis antigen 82;
DE Short=CT82;
DE AltName: Full=Fibrous sheath protein of 95 kDa;
DE Short=FSP95;
DE AltName: Full=Fibrousheathin I;
DE AltName: Full=Fibrousheathin-1;
DE AltName: Full=Protein kinase A-anchoring protein 3;
DE Short=PRKA3;
DE AltName: Full=Sperm oocyte-binding protein;
GN Name=AKAP3; Synonyms=AKAP110, SOB1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANTS GLU-118;
RP SER-464 AND LYS-525.
RC TISSUE=Testis;
RX PubMed=10334916; DOI=10.1006/bbrc.1999.0728;
RA Lefevre A., Duquenne C., Rousseau-Merck M.-F., Rogier E., Finaz C.;
RT "Cloning and characterization of SOB1, a new testis-specific cDNA encoding
RT a human sperm protein probably involved in oocyte recognition.";
RL Biochem. Biophys. Res. Commun. 259:60-66(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANTS GLU-118;
RP SER-464; THR-500 AND LYS-525.
RC TISSUE=Testis;
RX PubMed=10529264; DOI=10.1095/biolreprod61.5.1184;
RA Mandal A., Naaby-Hansen S., Wolkowicz M.J., Klotz K., Shetty J.,
RA Retief J.D., Coonrod S.A., Kinter M., Sherman N., Cesar F.,
RA Flickinger C.J., Herr J.C.;
RT "FSP95, a testis-specific 95-kilodalton fibrous sheath antigen that
RT undergoes tyrosine phosphorylation in capacitated human spermatozoa.";
RL Biol. Reprod. 61:1184-1197(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-464 AND LYS-525.
RC TISSUE=Testis;
RX PubMed=10319321; DOI=10.1210/mend.13.5.0278;
RA Vijayaraghavan S., Liberty G.A., Mohan J., Winfrey V.P., Olson G.E.,
RA Carr D.W.;
RT "Isolation and molecular characterization of AKAP110, a novel, sperm-
RT specific protein kinase A-anchoring protein.";
RL Mol. Endocrinol. 13:705-717(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-118.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-118.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH ROPN1 AND ROPN1L, AND MUTAGENESIS OF LEU-131.
RX PubMed=11278869; DOI=10.1074/jbc.m011252200;
RA Carr D.W., Fujita A., Stentz C.L., Liberty G.A., Olson G.E., Narumiya S.;
RT "Identification of sperm-specific proteins that interact with A-kinase
RT anchoring proteins in a manner similar to the type II regulatory subunit of
RT PKA.";
RL J. Biol. Chem. 276:17332-17338(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-208; SER-403;
RP TYR-404; SER-635 AND SER-636, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Sperm;
RX PubMed=12509440; DOI=10.1074/jbc.m202325200;
RA Ficarro S., Chertihin O., Westbrook V.A., White F., Jayes F., Kalab P.,
RA Marto J.A., Shabanowitz J., Herr J.C., Hunt D.F., Visconti P.E.;
RT "Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine
RT phosphorylation of a kinase-anchoring protein 3 and valosin-containing
RT protein/p97 during capacitation.";
RL J. Biol. Chem. 278:11579-11589(2003).
RN [9]
RP INTERACTION WITH QRICH2.
RX PubMed=30683861; DOI=10.1038/s41467-018-08182-x;
RA Shen Y., Zhang F., Li F., Jiang X., Yang Y., Li X., Li W., Wang X.,
RA Cheng J., Liu M., Zhang X., Yuan G., Pei X., Cai K., Hu F., Sun J., Yan L.,
RA Tang L., Jiang C., Tu W., Xu J., Wu H., Kong W., Li S., Wang K., Sheng K.,
RA Zhao X., Yue H., Yang X., Xu W.;
RT "Loss-of-function mutations in QRICH2 cause male infertility with multiple
RT morphological abnormalities of the sperm flagella.";
RL Nat. Commun. 10:433-433(2019).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-831.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May function as a regulator of both motility- and head-
CC associated functions such as capacitation and the acrosome reaction.
CC -!- SUBUNIT: Interacts with ROPN1 AND ROPN1L. Interacts with QRICH2
CC (PubMed:30683861). {ECO:0000269|PubMed:11278869,
CC ECO:0000269|PubMed:30683861}.
CC -!- INTERACTION:
CC O75969; Q7Z569: BRAP; NbExp=2; IntAct=EBI-9033101, EBI-349900;
CC O75969; P13861: PRKAR2A; NbExp=2; IntAct=EBI-9033101, EBI-2556122;
CC O75969; Q9BZX4: ROPN1B; NbExp=2; IntAct=EBI-9033101, EBI-9033148;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000250}. Note=Ribs of the fibrous sheath in the principal piece
CC of the sperm tail. Dorsal margin of the acrosomal segment.
CC -!- TISSUE SPECIFICITY: Testis specific; only expressed in spermatids.
CC -!- DOMAIN: RII-binding site, predicted to form an amphipathic helix, could
CC participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC -!- SIMILARITY: Belongs to the AKAP110 family. {ECO:0000305}.
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DR EMBL; U85715; AAD21218.1; -; mRNA.
DR EMBL; AF087003; AAC35854.1; -; mRNA.
DR EMBL; AF093408; AAC63371.1; -; mRNA.
DR EMBL; AK292451; BAF85140.1; -; mRNA.
DR EMBL; AC005832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047535; AAH47535.1; -; mRNA.
DR CCDS; CCDS8531.1; -.
DR RefSeq; NP_001265238.1; NM_001278309.1.
DR RefSeq; NP_006413.3; NM_006422.3.
DR RefSeq; XP_005253721.1; XM_005253664.2.
DR RefSeq; XP_011519210.1; XM_011520908.1.
DR RefSeq; XP_011519211.1; XM_011520909.1.
DR RefSeq; XP_011519212.1; XM_011520910.2.
DR AlphaFoldDB; O75969; -.
DR SMR; O75969; -.
DR BioGRID; 115817; 10.
DR IntAct; O75969; 5.
DR STRING; 9606.ENSP00000228850; -.
DR iPTMnet; O75969; -.
DR PhosphoSitePlus; O75969; -.
DR BioMuta; AKAP3; -.
DR EPD; O75969; -.
DR jPOST; O75969; -.
DR MassIVE; O75969; -.
DR PaxDb; O75969; -.
DR PeptideAtlas; O75969; -.
DR PRIDE; O75969; -.
DR ProteomicsDB; 50329; -.
DR Antibodypedia; 22296; 188 antibodies from 33 providers.
DR DNASU; 10566; -.
DR Ensembl; ENST00000228850.6; ENSP00000228850.1; ENSG00000111254.8.
DR Ensembl; ENST00000545990.6; ENSP00000440994.1; ENSG00000111254.8.
DR GeneID; 10566; -.
DR KEGG; hsa:10566; -.
DR MANE-Select; ENST00000228850.6; ENSP00000228850.1; NM_001278309.2; NP_001265238.2.
DR CTD; 10566; -.
DR DisGeNET; 10566; -.
DR GeneCards; AKAP3; -.
DR HGNC; HGNC:373; AKAP3.
DR HPA; ENSG00000111254; Tissue enriched (testis).
DR MIM; 604689; gene.
DR neXtProt; NX_O75969; -.
DR OpenTargets; ENSG00000111254; -.
DR PharmGKB; PA24667; -.
DR VEuPathDB; HostDB:ENSG00000111254; -.
DR eggNOG; ENOG502SM7F; Eukaryota.
DR GeneTree; ENSGT00940000153313; -.
DR HOGENOM; CLU_017072_0_0_1; -.
DR InParanoid; O75969; -.
DR OMA; ENFICDS; -.
DR OrthoDB; 221175at2759; -.
DR PhylomeDB; O75969; -.
DR TreeFam; TF105403; -.
DR PathwayCommons; O75969; -.
DR SignaLink; O75969; -.
DR BioGRID-ORCS; 10566; 21 hits in 1070 CRISPR screens.
DR ChiTaRS; AKAP3; human.
DR GeneWiki; AKAP3; -.
DR GenomeRNAi; 10566; -.
DR Pharos; O75969; Tbio.
DR PRO; PR:O75969; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O75969; protein.
DR Bgee; ENSG00000111254; Expressed in left testis and 103 other tissues.
DR ExpressionAtlas; O75969; baseline and differential.
DR Genevisible; O75969; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0035686; C:sperm fibrous sheath; IEA:Ensembl.
DR GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
DR GO; GO:0097228; C:sperm principal piece; IDA:UniProtKB.
DR GO; GO:0051018; F:protein kinase A binding; IBA:GO_Central.
DR GO; GO:0007340; P:acrosome reaction; TAS:ProtInc.
DR GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0007338; P:single fertilization; TAS:ProtInc.
DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IEA:Ensembl.
DR InterPro; IPR020799; AKAP_110.
DR InterPro; IPR018292; AKAP_110_C.
DR InterPro; IPR018459; RII-bd_1.
DR InterPro; IPR008382; SPHK1-interactor_AKAP_110.
DR PANTHER; PTHR10226; PTHR10226; 1.
DR Pfam; PF05716; AKAP_110; 1.
DR Pfam; PF10522; RII_binding_1; 1.
DR SMART; SM00807; AKAP_110; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Direct protein sequencing; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..853
FT /note="A-kinase anchor protein 3"
FT /id="PRO_0000064526"
FT REGION 124..137
FT /note="PKA-RII subunit binding domain"
FT REGION 188..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:12509440"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:12509440"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:12509440"
FT MOD_RES 404
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:12509440"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:12509440"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:12509440"
FT VARIANT 118
FT /note="G -> E (in dbSNP:rs2072355)"
FT /evidence="ECO:0000269|PubMed:10334916,
FT ECO:0000269|PubMed:10529264, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_055488"
FT VARIANT 464
FT /note="T -> S (in dbSNP:rs11063266)"
FT /evidence="ECO:0000269|PubMed:10319321,
FT ECO:0000269|PubMed:10334916, ECO:0000269|PubMed:10529264"
FT /id="VAR_060730"
FT VARIANT 500
FT /note="I -> T (in dbSNP:rs12366671)"
FT /evidence="ECO:0000269|PubMed:10529264"
FT /id="VAR_055489"
FT VARIANT 525
FT /note="E -> K (in dbSNP:rs1990312)"
FT /evidence="ECO:0000269|PubMed:10319321,
FT ECO:0000269|PubMed:10334916, ECO:0000269|PubMed:10529264"
FT /id="VAR_061000"
FT VARIANT 661
FT /note="I -> T (in dbSNP:rs1990313)"
FT /id="VAR_055490"
FT VARIANT 700
FT /note="S -> F (in dbSNP:rs2041291)"
FT /id="VAR_055491"
FT VARIANT 700
FT /note="S -> P (in dbSNP:rs2041290)"
FT /id="VAR_059112"
FT VARIANT 725
FT /note="S -> L (in dbSNP:rs2072357)"
FT /id="VAR_055492"
FT VARIANT 831
FT /note="R -> C (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs143517596)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036428"
FT MUTAGEN 131
FT /note="L->P: Abolishes interaction with ROPN1."
FT /evidence="ECO:0000269|PubMed:11278869"
FT CONFLICT 272
FT /note="E -> D (in Ref. 1; AAD21218)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="S -> G (in Ref. 2; AAC35854)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="E -> V (in Ref. 2; AAC35854)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="K -> N (in Ref. 2; AAC35854)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="F -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="S -> L (in Ref. 2; AAC35854)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 853 AA; 94751 MW; CFDEA26922B5A86E CRC64;
MSEKVDWLQS QNGVCKVDVY SPGDNQAQDW KMDTSTDPVR VLSWLRRDLE KSTAEFQDVR
FKPGESFGGE TSNSGDPHKG FSVDYYNTTT KGTPERLHFE MTHKEIPCQG PRAQLGNGSS
VDEVSFYANR LTNLVIAMAR KEINEKIDGS ENKCVYQSLY MGNEPTPTKS LSKIASELVN
ETVSACSRNA APDKAPGSGD RVSGSSQSPP NLKYKSTLKI KESTKERQGP DDKPPSKKSF
FYKEVFESRN GDYAREGGRF FPRERKRFRG QERPDDFTAS VSEGIMTYAN SVVSDMMVSI
MKTLKIQVKD TTIATILLKK VLLKHAKEVV SDLIDSFLRN LHSVTGTLMT DTQFVSAVKR
TVFSHGSQKA TDIMDAMLRK LYNVMFAKKV PEHVRKAQDK AESYSLISMK GMGDPKNRNV
NFAMKSETKL REKMYSEPKS EEETCAKTLG EHIIKEGLTL WHKTQQKECK SLGFQHAAFE
APNTQRKPAS DISFEYPEDI GNLSLPPYPP EKPENFMYDS DSWAEDLIVS ALLLIQYHLA
QGGRRDARSF VEAAGTTNFP ANEPPVAPDE SCLKSAPIVG DQEQAEKKDL RSVFFNFIRN
LLSETIFKRD QSPEPKVPEQ PVKEDRKLCE RPLASSPPRL YEDDETPGAL SGLTKMAVSQ
IDGHMSGQMV EHLMNSVMKL CVIIAKSCDA SLAELGDDKS GDASRLTSAF PDSLYECLPA
KGTGSAEAVL QNAYQAIHNE MRGTSGQPPE GCAAPTVIVS NHNLTDTVQN KQLQAVLQWV
AASELNVPIL YFAGDDEGIQ EKLLQLSAAA VDKGCSVGEV LQSVLRYEKE RQLNEAVGNV
TPLQLLDWLM VNL
